Migrastatics-Anti-metastatic and Anti-invasion Drugs: Promises and Challenges
Jazyk angličtina Země Spojené státy americké Médium print
Typ dokumentu časopisecké články, přehledy, práce podpořená grantem
Grantová podpora
12065
Cancer Research UK - United Kingdom
24478
Cancer Research UK - United Kingdom
PubMed
28670628
PubMed Central
PMC5482322
DOI
10.1016/j.trecan.2017.04.008
PII: S2405-8033(17)30085-7
Knihovny.cz E-zdroje
- Klíčová slova
- contractility, invasion, metastasis, migrastatics, solid cancer, treatment,
- MeSH
- chemorezistence MeSH
- cílená molekulární terapie MeSH
- lidé MeSH
- metastázy nádorů farmakoterapie MeSH
- nádorové biomarkery MeSH
- nádory farmakoterapie etiologie metabolismus patologie MeSH
- objevování léků * MeSH
- pohyb buněk účinky léků MeSH
- protinádorové látky chemie farmakologie terapeutické užití MeSH
- signální transdukce účinky léků MeSH
- synergismus léků MeSH
- zvířata MeSH
- Check Tag
- lidé MeSH
- zvířata MeSH
- Publikační typ
- časopisecké články MeSH
- práce podpořená grantem MeSH
- přehledy MeSH
- Názvy látek
- nádorové biomarkery MeSH
- protinádorové látky MeSH
In solid cancers, invasion and metastasis account for more than 90% of mortality. However, in the current armory of anticancer therapies, a specific category of anti-invasion and antimetastatic drugs is missing. Here, we coin the term 'migrastatics' for drugs interfering with all modes of cancer cell invasion and metastasis, to distinguish this class from conventional cytostatic drugs, which are mainly directed against cell proliferation. We define actin polymerization and contractility as target mechanisms for migrastatics, and review candidate migrastatic drugs. Critical assessment of these antimetastatic agents is warranted, because they may define new options for the treatment of solid cancers.
Ayurveda Molecular Modeling Hyderabad Telangana India
Central European Institute of Technology Brno University of Technology Brno Czech Republic
Charles University Department of Internal Medicine 3rd Faculty of Medicine Prague Czech Republic
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Prick J. Clonal heterogeneity as a driver of disease variability in the evolution of myeloproliferative neoplasms. Exp. Hematol. 2014;42:841–851. PubMed
Nowell P.C. The clonal evolution of tumor cell populations. Science. 1976;194:23–28. PubMed
Brenner M.K. Hematological malignancies. FASEB J. 1997;11:640–648. PubMed
Fernandes M. Translation in solid cancer: are size-based response criteria an anachronism? Clin. Transl. Oncol. 2015;17:1–10. PubMed
Sleeman J., Steeg P.S. Cancer metastasis as a therapeutic target. Eur. J. Cancer. 2010;46:1177–1180. PubMed PMC
Hanahan D., Weinberg R.A. Hallmarks of cancer: the next generation. Cell. 2011;144:646–674. PubMed
Lazebnik Y. What are the hallmarks of cancer? Nat. Rev. Cancer. 2010;10:232–233. PubMed
Rösel D. Drugs for solid cancer: the productivity crisis prompts a rethink. Onco. Targets. Ther. 2013;6:767–777. PubMed PMC
Seymour L. iRECIST: guidelines for response criteria for use in trials testing immunotherapeutics. Lancet Oncol. 2017;18:e143–e152. PubMed PMC
Cragg G.M. Impact of natural products on developing new anti-cancer agents. Chem. Rev. 2009;109:3012–3043. PubMed
Block K.I. Designing a broad-spectrum integrative approach for cancer prevention and treatment. Semin. Cancer Biol. 2015;35(Suppl):S276–S304. PubMed PMC
Bronsert P. Cancer cell invasion and EMT marker expression: a three-dimensional study of the human cancer–host interface. J Pathol. 2014;234:410–422. PubMed
Friedl P. Classifying collective cancer cell invasion. Nat. Cell Biol. 2012;14:777–783. PubMed
Panková K. The molecular mechanisms of transition between mesenchymal and amoeboid invasiveness in tumor cells. Cell. Mol. Life Sci. 2010;67:63–71. PubMed PMC
Clark A.G., Vignjevic D.M. Modes of cancer cell invasion and the role of the microenvironment. Curr. Opin. Cell Biol. 2015;36:13–22. PubMed
Friedl P., Wolf K. Tumour-cell invasion and migration: diversity and escape mechanisms. Nat. Rev. Cancer. 2003;3:362–374. PubMed
Wolf K. Compensation mechanism in tumor cell migration: mesenchymal-amoeboid transition after blocking of pericellular proteolysis. J. Cell Biol. 2003;160:267–277. PubMed PMC
Brábek J. The role of the tissue microenvironment in the regulation of cancer cell motility and invasion. Cell Commun. Signal. 2010;8:22. PubMed PMC
Sahai E., Marshall C.J. Differing modes of tumour cell invasion have distinct requirements for Rho/ROCK signalling and extracellular proteolysis. Nat. Cell Biol. 2003;5:711–719. PubMed
Sanz-Moreno V. Rac activation and inactivation control plasticity of tumor cell movement. Cell. 2008;135:510–523. PubMed
Noy R., Pollard J.W. Tumor-associated macrophages: from mechanisms to therapy. Immunity. 2016;41:49–61. PubMed PMC
Gillis N.K., McLeod H.L. The pharmacogenomics of drug resistance to protein kinase inhibitors. Drug Resist. Updat. 2016;28:28–42. PubMed PMC
Mitchison T.J., Cramer L.P. Actin-based cell motility and cell locomotion. Cell. 1996;84:371–379. PubMed
Fife C.M. Movers and shakers: cell cytoskeleton in cancer metastasis. Br. J. Pharmacol. 2014;171:5507–5523. PubMed PMC
Olson M.F., Sahai E. The actin cytoskeleton in cancer cell motility. Clin. Exp. Metastasis. 2009;26:273–287. PubMed
Tolde O. The structure of invadopodia in a complex 3D environment. Eur. J. Cell Biol. 2010;89:674–680. PubMed
Aratyn-Schaus Y. Dynamic and structural signatures of lamellar actomyosin force generation. Mol. Biol. Cell. 2011;22:1330–1339. PubMed PMC
Salbreux G. Actin cortex mechanics and cellular morphogenesis. Trends Cell Biol. 2012;22:536–545. PubMed
Levayer R., Lecuit T. Biomechanical regulation of contractility: spatial control and dynamics. Trends Cell Biol. 2012;22:61–81. PubMed
Amano M. Phosphorylation and activation of myosin by Rho-associated kinase (Rho-kinase) J. Biol. Chem. 1996;271:20246–20249. PubMed
Kimura K. Regulation of myosin phosphatase by Rho and Rho-associated kinase (Rho-kinase) Science. 1996;273:245–248. PubMed
Wilkinson S. Cdc42-MRCK and Rho-ROCK signalling cooperate in myosin phosphorylation and cell invasion. Nat. Cell Biol. 2005;7:255–261. PubMed
Yamaguchi H., Condeelis J. Regulation of the actin cytoskeleton in cancer cell migration and invasion. Biochim. Biophys. Acta. 2007;1773:642–652. PubMed PMC
Gross S.R. Actin binding proteins: their ups and downs in metastatic life. Cell Adh. Migr. 2013;7:199–213. PubMed PMC
Dumontet C., Jordan M.A. Microtubule-binding agents: a dynamic field of cancer therapeutics. Nat. Rev. Drug Discov. 2010;9:790–803. PubMed PMC
Trendowski M. Exploiting the cytoskeletal filaments of neoplastic cells to potentiate a novel therapeutic approach. Biochim. Biophys. Acta. 2014;1846:599–616. PubMed
Fenteany G., Zhu S. Small-molecule inhibitors of actin dynamics and cell motility. Curr. Top. Med. Chem. 2003;3:593–616. PubMed
Allingham J.S. Actin-targeting natural products: structures, properties and mechanisms of action. Cell. Mol. Life Sci. 2006;63:2119–2134. PubMed PMC
Hayot C. Characterization of the activities of actin-affecting drugs on tumor cell migration. Toxicol. Appl. Pharmacol. 2006;211:30–40. PubMed
Van Goietsenoven G. In vitro growth inhibitory effects of cytochalasins and derivatives in cancer cells. Planta Med. 2011;77:711–717. PubMed
Murray D. NET1-mediated RhoA activation facilitates lysophosphatidic acid-induced cell migration and invasion in gastric cancer. Br. J. Cancer. 2008;99:1322–1329. PubMed PMC
Sun W. Mechanistic adaptability of cancer cells strongly affects anti-migratory drug efficacy. J. R. Soc. Interface. 2014;11:20140638. PubMed PMC
Huang F.-Y. Cytochalasin D promotes pulmonary metastasis of B16 melanoma through expression of tissue factor. Oncol. Rep. 2013;30:478–484. PubMed
Singh J., Hood R.D. Effects of protein deficiency on the teratogenicity of cytochalasins in mice. Teratology. 1987;35:87–93. PubMed
Hagmar B., Ryd W. Tumor cell locomotion – a factor in metastasis formation? Influence of cytochalasin B on a tumor dissemination pattern. Int. J. Cancer. 1977;19:576–580. PubMed
Hart I.R. Effect of cytoskeleton-disrupting agents on the metastatic behavior of melanoma cells. J. Natl. Cancer Inst. 1980;64:891–900. PubMed
Bousquet P.F. Effects of cytochalasin B in culture and in vivo on murine Madison 109 lung carcinoma and on B16 melanoma. Cancer Res. 1990;50:1431–1439. PubMed
Bogyo D. Cytochalasin-B-induced immunosuppression of murine allogeneic anti-tumor response and the effect of recombinant human interleukin-2. Cancer Immunol. Immunother. 1991;32:400–405. PubMed PMC
Tannert R. Synthesis and structure-activity correlation of natural-product inspired cyclodepsipeptides stabilizing F-actin. J. Am. Chem. Soc. 2010;132:3063–3077. PubMed
Freitas V.M. The geodiamolide H, derived from Brazilian sponge Geodia corticostylifera, regulates actin cytoskeleton, migration and invasion of breast cancer cells cultured in three-dimensional environment. J. Cell. Physiol. 2008;216:583–594. PubMed
Yarmola E.G. Actin-latrunculin A structure and function. Differential modulation of actin-binding protein function by latrunculin A. J. Biol Chem. 2000;275:28120–28127. PubMed
Ahmed S.A. Latrunculin with a highly oxidized thiazolidinone ring: structure assignment and actin docking. Org. Lett. 2007;9:4773–4776. PubMed PMC
Nummela P. Thymosin beta4 is a determinant of the transformed phenotype and invasiveness of S-adenosylmethionine decarboxylase-transfected fibroblasts. Cancer Res. 2006;66:701–712. PubMed
Tolde O. Neoplastic progression of the human breast cancer cell line G3S1 is associated with elevation of cytoskeletal dynamics and upregulation of MT1-MMP. Int. J. Oncol. 2010;36:833–839. PubMed
Amornphimoltham P. Rab25 regulates invasion and metastasis in head and neck cancer. Clin. Cancer Res. 2013;19:1375–1388. PubMed PMC
Sayed K.A. El. Latrunculin A and its C-17-O-carbamates inhibit prostate tumor cell invasion and HIF-1 activation in breast tumor cells. J. Nat. Prod. 2008;71:396–402. PubMed PMC
Khanfar M.A. Semisynthetic latrunculin derivatives as inhibitors of metastatic breast cancer: biological evaluations, preliminary structure-activity relationship and molecular modeling studies. ChemMedChem. 2010;5:274–285. PubMed PMC
Konishi H. Latrunculin a has a strong anticancer effect in a peritoneal dissemination model of human gastric cancer in mice. Anticancer Res. 2009;29:2091–2097. PubMed
Bubb M.R. Jasplakinolide, a cytotoxic natural product, induces actin polymerization and competitively inhibits the binding of phalloidin to F-actin. J. Biol. Chem. 1994;269:14869–14871. PubMed
Takeuchi H. Jasplakinolide: interaction with radiation and hyperthermia in human prostate carcinoma and Lewis lung carcinoma. Cancer Chemother. Pharmacol. 1998;42:491–496. PubMed
Kunze B. Chondramides A approximately D, new antifungal and cytostatic depsipeptides from Chondromyces crocatus (Myxobacteria) Production, physico-chemical and biological properties. J. Antibiot. (Tokyo) 1995;48:1262–1266. PubMed
Menhofer M.H. The actin targeting compound Chondramide inhibits breast cancer metastasis via reduction of cellular contractility. PLoS One. 2014;9:e112542. PubMed PMC
Sorensen P.M. The natural product cucurbitacin E inhibits depolymerization of actin filaments. ACS Chem. Biol. 2012;7:1502–1508. PubMed PMC
Zhang T. Cucurbitacin E inhibits breast tumor metastasis by suppressing cell migration and invasion. Breast Cancer Res. Treat. 2012;135:445–458. PubMed
Rodriguez-Hernandez I. Rho, ROCK and actomyosin contractility in metastasis as drug targets. F1000Research. 2016;5 F1000 Faculty Rev-783. PubMed PMC
Kosla J. Metastasis of aggressive amoeboid sarcoma cells is dependent on Rho/ROCK/MLC signaling. Cell Commun. Signal. 2013;11:51. PubMed PMC
Sanz-Moreno V. ROCK and JAK1 signaling cooperate to control actomyosin contractility in tumor cells and stroma. Cancer Cell. 2011;20:229–245. PubMed
Stehn J.R. A novel class of anticancer compounds targets the actin cytoskeleton in tumor cells. Cancer Res. 2013;73:5169–5182. PubMed
Duxbury M.S. Inhibition of pancreatic adenocarcinoma cellular invasiveness by blebbistatin: a novel myosin II inhibitor. Biochem. Biophys. Res. Commun. 2004;313:992–997. PubMed
Arozarena I. Oncogenic BRAF induces melanoma cell invasion by downregulating the cGMP-specific phosphodiesterase PDE5A. Cancer Cell. 2011;19:45–57. PubMed
Kim J.H., Adelstein R.S. LPA(1)-induced migration requires nonmuscle myosin II light chain phosphorylation in breast cancer cells. J. Cell. Physiol. 2011;226:2881–2893. PubMed PMC
Derycke L. The role of non-muscle myosin IIA in aggregation and invasion of human MCF-7 breast cancer cells. Int. J. Dev. Biol. 2011;55:835–840. PubMed
Seifert S., Sontheimer H. Bradykinin enhances invasion of malignant glioma into the brain parenchyma by inducing cells to undergo amoeboid migration. J. Physiol. 2014;592:5109–5127. PubMed PMC
Totsukawa G. Distinct roles of ROCK (Rho-kinase) and MLCK in spatial regulation of MLC phosphorylation for assembly of stress fibers and focal adhesions in 3T3 fibroblasts. J. Cell Biol. 2000;150:797–806. PubMed PMC
Kaneko K. Myosin light chain kinase inhibitors can block invasion and adhesion of human pancreatic cancer cell lines. Pancreas. 2002;24:34–41. PubMed
Tohtong R. Dependence of metastatic cancer cell invasion on MLCK-catalyzed phosphorylation of myosin regulatory light chain. Prostate Cancer Prostatic Dis. 2003;6:212–216. PubMed
Gu L.-Z. Inhibiting myosin light chain kinase retards the growth of mammary and prostate cancer cells. Eur. J. Cancer. 2006;42:948–957. PubMed
Nakagawa O. ROCK-I and ROCK-II, two isoforms of Rho-associated coiled-coil forming protein serine/threonine kinase in mice. FEBS Lett. 1996;392:189–193. PubMed
Ying H. The Rho kinase inhibitor fasudil inhibits tumor progression in human and rat tumor models. Mol. Cancer Ther. 2006;5:2158–2164. PubMed
Ogata S. Fasudil inhibits lysophosphatidic acid-induced invasiveness of human ovarian cancer cells. Int. J. Gynecol. Cancer. 2009;19:1473–1480. PubMed
Zhu F. Rho kinase inhibitor fasudil suppresses migration and invasion though down-regulating the expression of VEGF in lung cancer cell line A549. Med. Oncol. 2011;28:565–571. PubMed
Deng L. Rho-kinase inhibitor, fasudil, suppresses glioblastoma cell line progression in vitro and in vivo. Cancer Biol. Ther. 2010;9:875–884. PubMed
Yang X. Effect of fasudil on growth, adhesion, invasion, and migration of 95D lung carcinoma cells in vitro. Can. J. Physiol. Pharmacol. 2010;88:874–879. PubMed
Yang X. The Rho-kinase inhibitor inhibits proliferation and metastasis of small cell lung cancer. Biomed. Pharmacother. 2012;66:221–227. PubMed
Hu K. Suppression of hepatocellular carcinoma invasion and metastasis by Rho-kinase inhibitor Fasudil through inhibition of BTBD7-ROCK2 signaling pathway. Zhong Nan Da Xue Xue Bao. Yi Xue Ban. 2014;39:1221–1227. PubMed
Moreira Carboni Sde S. HA-1077 inhibits cell migration/invasion of oral squamous cell carcinoma. Anticancer Drugs. 2015;26:923–930. PubMed
Nakashima S. Combination therapy of fasudil hydrochloride and ozagrel sodium for cerebral vasospasm following aneurysmal subarachnoid hemorrhage. Neurol. Med. Chir. (Tokyo) 1998;38:801–805. PubMed
Uehata M. Calcium sensitization of smooth muscle mediated by a Rho-associated protein kinase in hypertension. Nature. 1997;389:990–994. PubMed
Itoh K. An essential part for Rho-associated kinase in the transcellular invasion of tumor cells. Nat. Med. 1999;5:221–225. PubMed
Somlyo A.V. Rho-kinase inhibitor retards migration and in vivo dissemination of human prostate cancer cells. Biochem. Biophys. Res. Commun. 2000;269:652–659. PubMed
Takamura M. Inhibition of intrahepatic metastasis of human hepatocellular carcinoma by Rho-associated protein kinase inhibitor Y-27632. Hepatology. 2001;33:577–581. PubMed
Saurin J.-C. Bombesin stimulates invasion and migration of Isreco1 colon carcinoma cells in a Rho-dependent manner. Cancer Res. 2002;62:4829–4835. PubMed
Yoshioka K. A role for LIM kinase in cancer invasion. Proc. Natl. Acad. Sci. U. S. A. 2003;100:7247–7252. PubMed PMC
Wang D.-S. Enhancement of migration and invasion of hepatoma cells via a Rho GTPase signaling pathway. World J. Gastroenterol. 2004;10:299–302. PubMed PMC
Zhong W.-B. Lovastatin suppresses invasiveness of anaplastic thyroid cancer cells by inhibiting Rho geranylgeranylation and RhoA/ROCK signaling. Endocr. Relat. Cancer. 2005;12:615–629. PubMed
Lawler K. Mobility and invasiveness of metastatic esophageal cancer are potentiated by shear stress in a ROCK- and Ras-dependent manner. Am. J. Physiol. Cell Physiol. 2006;291:C668–C677. PubMed
Hakuma N. E1AF/PEA3 activates the Rho/Rho-associated kinase pathway to increase the malignancy potential of non-small-cell lung cancer cells. Cancer Res. 2005;65:10776–10782. PubMed
Xue F. Blockade of Rho/Rho-associated coiled coil-forming kinase signaling can prevent progression of hepatocellular carcinoma in matrix metalloproteinase-dependent manner. Hepatol. Res. 2008;38:810–817. PubMed
Routhier A. Pharmacological inhibition of Rho-kinase signaling with Y-27632 blocks melanoma tumor growth. Oncol. Rep. 2010;23:861–867. PubMed
Nakashima M., Lazo J.S. Phosphatase of regenerating liver-1 promotes cell migration and invasion and regulates filamentous actin dynamics. J. Pharmacol. Exp. Ther. 2010;334:627–633. PubMed PMC
Wang L. Autocrine motility factor receptor signaling pathway promotes cell invasion via activation of ROCK-2 in esophageal squamous cell cancer cells. Cancer Invest. 2010;28:993–1003. PubMed
Jeong K.J. The Rho/ROCK pathway for lysophosphatidic acid-induced proteolytic enzyme expression and ovarian cancer cell invasion. Oncogene. 2012;31:4279–4289. PubMed
Zhao M. Expression of serum response factor in gastric carcinoma and its molecular mechanisms involved in the regulation of the invasion and migration of SGC-7901 cells. Cancer Biother. Radiopharm. 2013;28:146–152. PubMed
de Toledo M. Cooperative anti-invasive effect of Cdc42/Rac1 activation and ROCK inhibition in SW620 colorectal cancer cells with elevated blebbing activity. PLoS One. 2012;7:e48344. PubMed PMC
An L. microRNA-124 inhibits migration and invasion by down-regulating ROCK1 in glioma. PLoS One. 2013;8:e69478. PubMed PMC
Zhang L. PTEN inhibits the invasion and metastasis of gastric cancer via downregulation of FAK expression. Cell. Signal. 2014;397:1–10. PubMed
Voorneveld P.W. Loss of SMAD4 alters BMP signaling to promote colorectal cancer cell metastasis via activation of Rho and ROCK. Gastroenterology. 2014;147:196–208. PubMed
Wang J. The effect of ROCK-1 activity change on the adhesive and invasive ability of Y79 retinoblastoma cells. BMC Cancer. 2014;14:89. PubMed PMC
Wang Z.-M. ROCK inhibitor Y-27632 inhibits the growth, migration, and invasion of Tca8113 and CAL-27 cells in tongue squamous cell carcinoma. Tumour Biol. 2016;37:3757–3764. PubMed
Salhia B. Inhibition of Rho-kinase affects astrocytoma morphology, motility, and invasion through activation of Rac1. Cancer Res. 2005;65:8792–8800. PubMed
Matsuoka T. RhoA/ROCK signaling mediates plasticity of scirrhous gastric carcinoma motility. Clin. Exp. Metastasis. 2011;28:627–636. PubMed
Sadok A. Rho kinase inhibitors block melanoma cell migration and inhibit metastasis. Cancer Res. 2015;75:2272–2284. PubMed
Wei L. Novel insights into the roles of Rho kinase in cancer. Arch. Immunol. Ther. Exp. (Warsz) 2016;64:259–278. PubMed PMC
Ikenoya M. Inhibition of Rho-kinase-induced myristoylated alanine-rich C kinase substrate (MARCKS) phosphorylation in human neuronal cells by H-1152, a novel and specific Rho-kinase inhibitor. J. Neurochem. 2002;81:9–16. PubMed
Fagan-Solis K.D. The RhoA pathway mediates MMP-2 and MMP-9-independent invasive behavior in a triple-negative breast cancer cell line. J. Cell. Biochem. 2013;114:1385–1394. PubMed
Nakajima M. Effect of Wf-536, a novel ROCK inhibitor, against metastasis of B16 melanoma. Cancer Chemother. Pharmacol. 2003;52:319–324. PubMed
Loge C. Rho-kinase inhibitors: pharmacomodulations on the lead compound Y-32885. J. Enzyme Inhib. Med. Chem. 2002;17:381–390. PubMed
Patel R.A. RKI-1447 is a potent inhibitor of the Rho-associated ROCK kinases with anti-invasive and antitumor activities in breast cancer. Cancer Res. 2012;72:5025–5034. PubMed PMC
Patel R.A. Identification of novel ROCK inhibitors with anti-migratory and anti-invasive activities. Oncogene. 2014;33:550–555. PubMed PMC
Unbekandt M. A novel small-molecule MRCK inhibitor blocks cancer cell invasion. Cell Commun. Signal. 2014;12:54. PubMed PMC
Kale V.P. A novel selective multikinase inhibitor of ROCK and MRCK effectively blocks cancer cell migration and invasion. Cancer Lett. 2014;4:1–12. PubMed PMC
Davies S.P. Specificity and mechanism of action of some commonly used protein kinase inhibitors. Biochem. J. 2000;351:95–105. PubMed PMC
Feng Y. Rho kinase (ROCK) inhibitors and their therapeutic potential. J. Med. Chem. 2016;59:2269–2300. PubMed
Papadatos-Pastos D. A first-in-human study of the dual ROCK I/II inhibitor, AT13148, in patients with advanced cancers. ASCO Annu. Meet. Proc. 2015;33:2566.
Schwab A., Stock C. Ion channels and transporters in tumour cell migration and invasion. Philos. Trans. R. Soc. Lond. B. Biol. Sci. 2014;369:20130102. PubMed PMC
The Lancet Oncology Cancer drug safety: time to re-focus on tackling adverse effects. Lancet Oncol. 2016;17:1463. PubMed
Steeg P.S. Targeting metastasis. Nat. Rev. Cancer. 2016;16:201–218. PubMed PMC
Scott V.R. New class of antifungal agents: jasplakinolide, a cyclodepsipeptide from the marine sponge, Jaspis species. Antimicrob. Agents Chemother. 1988;32:1154–1157. PubMed PMC
Hotulainen P., Hoogenraad C.C. Actin in dendritic spines: connecting dynamics to function. J. Cell Biol. 2010;189:619–629. PubMed PMC
Waschke J. Regulation of actin dynamics is critical for endothelial barrier functions. Am. J. Physiol. − Hear. Circ. Physiol. 2005;288:1296–1305. PubMed
Tashiro E., Imoto M. Screening and target identification of bioactive compounds that modulate cell migration and autophagy. Bioorg. Med. Chem. 2016;24:3283–3290. PubMed
Lyubchenko T.A. The actin cytoskeleton and cytotoxic T lymphocytes: evidence for multiple roles that could affect granule exocytosis-dependent target cell killing. J. Physiol. 2003;547:835–847. PubMed PMC
Zanin-Zhorov A. Isoform-specific targeting of ROCK proteins in immune cells. Small GTPases. 2016;7:173–177. PubMed PMC
Teiti I. In vivo effects in melanoma of ROCK inhibition-induced FasL overexpression. Front. Oncol. 2015;5:156. PubMed PMC
Kumper S. Rho-associated kinase (ROCK) function is essential for cell cycle progression, senescence and tumorigenesis. eLife. 2016;5:e12994. PubMed PMC
Trendowski M. The real deal: using cytochalasin B in sonodynamic therapy to preferentially damage leukemia cells. Anticancer Res. 2014;34:2195–2202. PubMed
Trendowski M. The promise of sonodynamic therapy. Cancer Metastasis Rev. 2014;33:143–160. PubMed
Kolber M.A., Hill P. Vincristine potentiates cytochalasin B-induced DNA fragmentation in vitro. Cancer Chemother. Pharmacol. 1992;30:286–290. PubMed
Somers K.D., Murphey M.M. Multinucleation in response to cytochalasin B: a common feature in several human tumor cell lines. Cancer Res. 1982;42:2575–2578. PubMed
Holzinger A. Jasplakinolide: An actin-specific reagent that promotes actin polymerization. Methods Mol. Biol. 2001;161:109–120. PubMed
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